Parasitology Research vol. 90, no. 5, pp. 365 - 368
We purified the 17 kDa protein abundant in Clonorchis sinensis crude extracts. The N-terminal amino acid sequence of this protein was determined and an oligonucleotide probe synthesized. Using this probe, the cDNA encoding the protein was cloned and sequenced from the C. sinensis cDNA library. It was found to consist of a total of 150 amino acids and to have 41% conserved homology with the myoglobin of the trematodes Paramphistomum epiclitum and Isoparorchis hypselobagri. The gene product over-expressed in the bacterial system was purified and identified as the same molecule in the adult worms. BALB/c mouse sera raised against the adult 17 kDa protein revealed that this myoglobin was distributed throughout the parenchymal tissues except for the eggs and reproductive organs and that the protein may be involved in the survival of C. sinensis in the oxygen-depleted environment of the host.